HEADER HYDROLASE 09-NOV-05 2EYQ
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSCRIPTION-REPAIR COUPLING
TITLE 2 FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION-REPAIR COUPLING FACTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRCF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MFD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MFD, SF2 ATPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.DEACONESCU,S.A.DARST
REVDAT 3 14-FEB-24 2EYQ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EYQ 1 VERSN
REVDAT 1 28-FEB-06 2EYQ 0
JRNL AUTH A.M.DEACONESCU,A.L.CHAMBERS,A.J.SMITH,B.E.NICKELS,
JRNL AUTH 2 A.HOCHSCHILD,N.J.SAVERY,S.A.DARST
JRNL TITL STRUCTURAL BASIS FOR BACTERIAL TRANSCRIPTION-COUPLED DNA
JRNL TITL 2 REPAIR.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 124 507 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16469698
JRNL DOI 10.1016/J.CELL.2005.11.045
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 61185
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3083
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17853
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 90
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98166
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61409
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PENTAERYTHRITOL ETHOXYLATE 100 MM
REMARK 280 HEPES, PH 7.5 75MM AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 75.93500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.99500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.93500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 80.99500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 1148
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 3
REMARK 465 GLN B 4
REMARK 465 ALA B 1148
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 3 CG CD OE1 OE2
REMARK 470 ARG A 6 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 GLU A 225 CG CD OE1 OE2
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 ARG A 239 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 347 CG CD CE NZ
REMARK 470 GLN A 410 CG CD OE1 NE2
REMARK 470 VAL A 438 CG1 CG2
REMARK 470 ARG A 457 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 458 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 459 CG CD OE1 NE2
REMARK 470 ASP A 460 CG OD1 OD2
REMARK 470 SER A 461 OG
REMARK 470 ARG A 462 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 468 CG OD1 OD2
REMARK 470 THR A 469 OG1 CG2
REMARK 470 ARG A 472 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 537 CG CD OE1 OE2
REMARK 470 GLU A 538 CG CD OE1 OE2
REMARK 470 LYS A 560 CG CD CE NZ
REMARK 470 GLU A 567 CG CD OE1 OE2
REMARK 470 LYS A 743 CG CD CE NZ
REMARK 470 ASN A 748 CG OD1 ND2
REMARK 470 GLU A 800 CG CD OE1 OE2
REMARK 470 VAL A 819 CG1 CG2
REMARK 470 GLU A 820 CG CD OE1 OE2
REMARK 470 GLU A 961 CG CD OE1 OE2
REMARK 470 SER A 993 OG
REMARK 470 LEU A 994 CG CD1 CD2
REMARK 470 ASP A 996 CG OD1 OD2
REMARK 470 LEU A 997 CG CD1 CD2
REMARK 470 THR A 998 OG1 CG2
REMARK 470 SER A 999 OG
REMARK 470 GLN A1000 CG CD OE1 NE2
REMARK 470 GLN A1001 CG CD OE1 NE2
REMARK 470 LYS A1072 CG CD CE NZ
REMARK 470 LYS A1092 CG CD CE NZ
REMARK 470 GLU A1127 CG CD OE1 OE2
REMARK 470 LYS A1129 CG CD CE NZ
REMARK 470 TYR B 5 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 6 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 9 CG CD1 CD2
REMARK 470 VAL B 11 CG1 CG2
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LEU B 19 CG CD1 CD2
REMARK 470 GLU B 21 CG CD OE1 OE2
REMARK 470 LEU B 22 CG CD1 CD2
REMARK 470 THR B 29 OG1 CG2
REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 53 CG CD1 CD2
REMARK 470 LYS B 221 CG CD CE NZ
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 ARG B 239 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 284 CG OD1 ND2
REMARK 470 ASN B 305 CG OD1 ND2
REMARK 470 LYS B 332 CG CD CE NZ
REMARK 470 LYS B 340 CG CD CE NZ
REMARK 470 GLU B 342 CG CD OE1 OE2
REMARK 470 HIS B 343 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 344 CG CD1 CD2
REMARK 470 LEU B 353 CG CD1 CD2
REMARK 470 GLN B 356 CG CD OE1 NE2
REMARK 470 ASP B 360 CG OD1 OD2
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 SER B 388 OG
REMARK 470 SER B 391 OG
REMARK 470 GLN B 410 CG CD OE1 NE2
REMARK 470 ARG B 414 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 415 CG CD1 CD2
REMARK 470 GLU B 417 CG CD OE1 OE2
REMARK 470 SER B 419 OG
REMARK 470 ASP B 420 CG OD1 OD2
REMARK 470 ARG B 421 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 423 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 424 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 425 CG CD1 CD2
REMARK 470 GLU B 431 CG CD OE1 OE2
REMARK 470 VAL B 435 CG1 CG2
REMARK 470 ASP B 436 CG OD1 OD2
REMARK 470 VAL B 438 CG1 CG2
REMARK 470 ARG B 439 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 444 CG1 CG2 CD1
REMARK 470 ARG B 456 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 457 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 458 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 460 CG OD1 OD2
REMARK 470 SER B 461 OG
REMARK 470 ARG B 462 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 538 CG CD OE1 OE2
REMARK 470 GLU B 559 CG CD OE1 OE2
REMARK 470 GLU B 579 CG CD OE1 OE2
REMARK 470 ASP B 671 OD1 OD2
REMARK 470 LYS B 743 CG CD CE NZ
REMARK 470 ASN B 748 CG OD1 ND2
REMARK 470 ASN B 817 CG OD1 ND2
REMARK 470 VAL B 819 CG1 CG2
REMARK 470 GLU B 820 CG CD OE1 OE2
REMARK 470 GLU B 962 CG CD OE1 OE2
REMARK 470 SER B 993 OG
REMARK 470 LEU B 994 CG CD1 CD2
REMARK 470 ASP B 996 CG OD1 OD2
REMARK 470 THR B 998 OG1 CG2
REMARK 470 GLN B1000 CG CD OE1 NE2
REMARK 470 LYS B1092 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N GLY B 940 O1S EPE B 1151 2.11
REMARK 500 OG SER A 82 O ALA A 255 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 179 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 414 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 414 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 PRO B 41 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 GLY B 422 N - CA - C ANGL. DEV. = 21.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 17 59.18 -151.37
REMARK 500 GLU A 21 75.25 43.47
REMARK 500 THR A 23 -127.76 -123.75
REMARK 500 ALA A 25 16.69 -56.76
REMARK 500 ALA A 26 -70.16 -59.40
REMARK 500 ILE A 34 -8.47 -53.48
REMARK 500 HIS A 38 100.59 163.89
REMARK 500 THR A 63 146.42 -171.90
REMARK 500 LYS A 132 -12.66 -27.77
REMARK 500 VAL A 156 91.40 67.82
REMARK 500 ARG A 165 72.43 -151.75
REMARK 500 LEU A 182 -84.94 -72.40
REMARK 500 ASP A 183 115.92 94.18
REMARK 500 ASP A 186 80.78 38.73
REMARK 500 ASP A 187 1.32 47.79
REMARK 500 ASP A 190 -83.10 -68.43
REMARK 500 GLN A 200 -8.80 80.00
REMARK 500 LEU A 203 -114.26 -89.59
REMARK 500 PRO A 213 -175.29 -55.34
REMARK 500 GLU A 216 57.76 -98.67
REMARK 500 PHE A 217 128.41 162.15
REMARK 500 ASP A 220 179.76 -54.71
REMARK 500 SER A 229 -72.28 -55.27
REMARK 500 ASP A 240 120.03 -22.06
REMARK 500 LYS A 250 4.12 -69.64
REMARK 500 PRO A 254 171.70 -56.60
REMARK 500 TYR A 259 39.20 -88.15
REMARK 500 TRP A 260 4.02 -153.60
REMARK 500 LEU A 263 -16.89 -48.58
REMARK 500 LEU A 272 -36.71 -35.32
REMARK 500 SER A 274 -17.22 -48.53
REMARK 500 PRO A 277 170.52 -57.96
REMARK 500 ASN A 279 35.88 -88.03
REMARK 500 ALA A 292 -35.56 -39.40
REMARK 500 ARG A 336 111.58 -160.72
REMARK 500 THR A 346 73.07 -52.11
REMARK 500 ALA A 351 -60.52 -127.55
REMARK 500 ASN A 352 66.36 75.70
REMARK 500 LEU A 358 156.66 -44.99
REMARK 500 PRO A 359 -175.24 -69.20
REMARK 500 VAL A 386 106.00 34.66
REMARK 500 PRO A 409 159.64 -44.62
REMARK 500 ILE A 412 -169.92 -110.84
REMARK 500 MET A 413 -46.62 -147.72
REMARK 500 THR A 437 -74.83 -51.54
REMARK 500 VAL A 438 -44.19 -25.64
REMARK 500 ASN A 440 77.84 44.35
REMARK 500 ARG A 453 171.90 -55.29
REMARK 500 SER A 461 -39.28 -23.12
REMARK 500 ASP A 468 -79.32 -60.11
REMARK 500
REMARK 500 THIS ENTRY HAS 206 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1152
DBREF 2EYQ A 1 1148 UNP P30958 MFD_ECOLI 1 1148
DBREF 2EYQ B 1 1148 UNP P30958 MFD_ECOLI 1 1148
SEQADV 2EYQ GLY A -2 UNP P30958 CLONING ARTIFACT
SEQADV 2EYQ PRO A -1 UNP P30958 CLONING ARTIFACT
SEQADV 2EYQ HIS A 0 UNP P30958 CLONING ARTIFACT
SEQADV 2EYQ GLY B -2 UNP P30958 CLONING ARTIFACT
SEQADV 2EYQ PRO B -1 UNP P30958 CLONING ARTIFACT
SEQADV 2EYQ HIS B 0 UNP P30958 CLONING ARTIFACT
SEQRES 1 A 1151 GLY PRO HIS MET PRO GLU GLN TYR ARG TYR THR LEU PRO
SEQRES 2 A 1151 VAL LYS ALA GLY GLU GLN ARG LEU LEU GLY GLU LEU THR
SEQRES 3 A 1151 GLY ALA ALA CYS ALA THR LEU VAL ALA GLU ILE ALA GLU
SEQRES 4 A 1151 ARG HIS ALA GLY PRO VAL VAL LEU ILE ALA PRO ASP MET
SEQRES 5 A 1151 GLN ASN ALA LEU ARG LEU HIS ASP GLU ILE SER GLN PHE
SEQRES 6 A 1151 THR ASP GLN MET VAL MET ASN LEU ALA ASP TRP GLU THR
SEQRES 7 A 1151 LEU PRO TYR ASP SER PHE SER PRO HIS GLN ASP ILE ILE
SEQRES 8 A 1151 SER SER ARG LEU SER THR LEU TYR GLN LEU PRO THR MET
SEQRES 9 A 1151 GLN ARG GLY VAL LEU ILE VAL PRO VAL ASN THR LEU MET
SEQRES 10 A 1151 GLN ARG VAL CYS PRO HIS SER PHE LEU HIS GLY HIS ALA
SEQRES 11 A 1151 LEU VAL MET LYS LYS GLY GLN ARG LEU SER ARG ASP ALA
SEQRES 12 A 1151 LEU ARG THR GLN LEU ASP SER ALA GLY TYR ARG HIS VAL
SEQRES 13 A 1151 ASP GLN VAL MET GLU HIS GLY GLU TYR ALA THR ARG GLY
SEQRES 14 A 1151 ALA LEU LEU ASP LEU PHE PRO MET GLY SER GLU LEU PRO
SEQRES 15 A 1151 TYR ARG LEU ASP PHE PHE ASP ASP GLU ILE ASP SER LEU
SEQRES 16 A 1151 ARG VAL PHE ASP VAL ASP SER GLN ARG THR LEU GLU GLU
SEQRES 17 A 1151 VAL GLU ALA ILE ASN LEU LEU PRO ALA HIS GLU PHE PRO
SEQRES 18 A 1151 THR ASP LYS ALA ALA ILE GLU LEU PHE ARG SER GLN TRP
SEQRES 19 A 1151 ARG ASP THR PHE GLU VAL LYS ARG ASP PRO GLU HIS ILE
SEQRES 20 A 1151 TYR GLN GLN VAL SER LYS GLY THR LEU PRO ALA GLY ILE
SEQRES 21 A 1151 GLU TYR TRP GLN PRO LEU PHE PHE SER GLU PRO LEU PRO
SEQRES 22 A 1151 PRO LEU PHE SER TYR PHE PRO ALA ASN THR LEU LEU VAL
SEQRES 23 A 1151 ASN THR GLY ASP LEU GLU THR SER ALA GLU ARG PHE GLN
SEQRES 24 A 1151 ALA ASP THR LEU ALA ARG PHE GLU ASN ARG GLY VAL ASP
SEQRES 25 A 1151 PRO MET ARG PRO LEU LEU PRO PRO GLN SER LEU TRP LEU
SEQRES 26 A 1151 ARG VAL ASP GLU LEU PHE SER GLU LEU LYS ASN TRP PRO
SEQRES 27 A 1151 ARG VAL GLN LEU LYS THR GLU HIS LEU PRO THR LYS ALA
SEQRES 28 A 1151 ALA ASN ALA ASN LEU GLY PHE GLN LYS LEU PRO ASP LEU
SEQRES 29 A 1151 ALA VAL GLN ALA GLN GLN LYS ALA PRO LEU ASP ALA LEU
SEQRES 30 A 1151 ARG LYS PHE LEU GLU THR PHE ASP GLY PRO VAL VAL PHE
SEQRES 31 A 1151 SER VAL GLU SER GLU GLY ARG ARG GLU ALA LEU GLY GLU
SEQRES 32 A 1151 LEU LEU ALA ARG ILE LYS ILE ALA PRO GLN ARG ILE MET
SEQRES 33 A 1151 ARG LEU ASP GLU ALA SER ASP ARG GLY ARG TYR LEU MET
SEQRES 34 A 1151 ILE GLY ALA ALA GLU HIS GLY PHE VAL ASP THR VAL ARG
SEQRES 35 A 1151 ASN LEU ALA LEU ILE CYS GLU SER ASP LEU LEU GLY GLU
SEQRES 36 A 1151 ARG VAL ALA ARG ARG ARG GLN ASP SER ARG ARG THR ILE
SEQRES 37 A 1151 ASN PRO ASP THR LEU ILE ARG ASN LEU ALA GLU LEU HIS
SEQRES 38 A 1151 ILE GLY GLN PRO VAL VAL HIS LEU GLU HIS GLY VAL GLY
SEQRES 39 A 1151 ARG TYR ALA GLY MET THR THR LEU GLU ALA GLY GLY ILE
SEQRES 40 A 1151 THR GLY GLU TYR LEU MET LEU THR TYR ALA ASN ASP ALA
SEQRES 41 A 1151 LYS LEU TYR VAL PRO VAL SER SER LEU HIS LEU ILE SER
SEQRES 42 A 1151 ARG TYR ALA GLY GLY ALA GLU GLU ASN ALA PRO LEU HIS
SEQRES 43 A 1151 LYS LEU GLY GLY ASP ALA TRP SER ARG ALA ARG GLN LYS
SEQRES 44 A 1151 ALA ALA GLU LYS VAL ARG ASP VAL ALA ALA GLU LEU LEU
SEQRES 45 A 1151 ASP ILE TYR ALA GLN ARG ALA ALA LYS GLU GLY PHE ALA
SEQRES 46 A 1151 PHE LYS HIS ASP ARG GLU GLN TYR GLN LEU PHE CYS ASP
SEQRES 47 A 1151 SER PHE PRO PHE GLU THR THR PRO ASP GLN ALA GLN ALA
SEQRES 48 A 1151 ILE ASN ALA VAL LEU SER ASP MET CYS GLN PRO LEU ALA
SEQRES 49 A 1151 MET ASP ARG LEU VAL CYS GLY ASP VAL GLY PHE GLY LYS
SEQRES 50 A 1151 THR GLU VAL ALA MET ARG ALA ALA PHE LEU ALA VAL ASP
SEQRES 51 A 1151 ASN HIS LYS GLN VAL ALA VAL LEU VAL PRO THR THR LEU
SEQRES 52 A 1151 LEU ALA GLN GLN HIS TYR ASP ASN PHE ARG ASP ARG PHE
SEQRES 53 A 1151 ALA ASN TRP PRO VAL ARG ILE GLU MET ILE SER ARG PHE
SEQRES 54 A 1151 ARG SER ALA LYS GLU GLN THR GLN ILE LEU ALA GLU VAL
SEQRES 55 A 1151 ALA GLU GLY LYS ILE ASP ILE LEU ILE GLY THR HIS LYS
SEQRES 56 A 1151 LEU LEU GLN SER ASP VAL LYS PHE LYS ASP LEU GLY LEU
SEQRES 57 A 1151 LEU ILE VAL ASP GLU GLU HIS ARG PHE GLY VAL ARG HIS
SEQRES 58 A 1151 LYS GLU ARG ILE LYS ALA MET ARG ALA ASN VAL ASP ILE
SEQRES 59 A 1151 LEU THR LEU THR ALA THR PRO ILE PRO ARG THR LEU ASN
SEQRES 60 A 1151 MET ALA MET SER GLY MET ARG ASP LEU SER ILE ILE ALA
SEQRES 61 A 1151 THR PRO PRO ALA ARG ARG LEU ALA VAL LYS THR PHE VAL
SEQRES 62 A 1151 ARG GLU TYR ASP SER MET VAL VAL ARG GLU ALA ILE LEU
SEQRES 63 A 1151 ARG GLU ILE LEU ARG GLY GLY GLN VAL TYR TYR LEU TYR
SEQRES 64 A 1151 ASN ASP VAL GLU ASN ILE GLN LYS ALA ALA GLU ARG LEU
SEQRES 65 A 1151 ALA GLU LEU VAL PRO GLU ALA ARG ILE ALA ILE GLY HIS
SEQRES 66 A 1151 GLY GLN MET ARG GLU ARG GLU LEU GLU ARG VAL MET ASN
SEQRES 67 A 1151 ASP PHE HIS HIS GLN ARG PHE ASN VAL LEU VAL CYS THR
SEQRES 68 A 1151 THR ILE ILE GLU THR GLY ILE ASP ILE PRO THR ALA ASN
SEQRES 69 A 1151 THR ILE ILE ILE GLU ARG ALA ASP HIS PHE GLY LEU ALA
SEQRES 70 A 1151 GLN LEU HIS GLN LEU ARG GLY ARG VAL GLY ARG SER HIS
SEQRES 71 A 1151 HIS GLN ALA TYR ALA TRP LEU LEU THR PRO HIS PRO LYS
SEQRES 72 A 1151 ALA MET THR THR ASP ALA GLN LYS ARG LEU GLU ALA ILE
SEQRES 73 A 1151 ALA SER LEU GLU ASP LEU GLY ALA GLY PHE ALA LEU ALA
SEQRES 74 A 1151 THR HIS ASP LEU GLU ILE ARG GLY ALA GLY GLU LEU LEU
SEQRES 75 A 1151 GLY GLU GLU GLN SER GLY SER MET GLU THR ILE GLY PHE
SEQRES 76 A 1151 SER LEU TYR MET GLU LEU LEU GLU ASN ALA VAL ASP ALA
SEQRES 77 A 1151 LEU LYS ALA GLY ARG GLU PRO SER LEU GLU ASP LEU THR
SEQRES 78 A 1151 SER GLN GLN THR GLU VAL GLU LEU ARG MET PRO SER LEU
SEQRES 79 A 1151 LEU PRO ASP ASP PHE ILE PRO ASP VAL ASN THR ARG LEU
SEQRES 80 A 1151 SER PHE TYR LYS ARG ILE ALA SER ALA LYS THR GLU ASN
SEQRES 81 A 1151 GLU LEU GLU GLU ILE LYS VAL GLU LEU ILE ASP ARG PHE
SEQRES 82 A 1151 GLY LEU LEU PRO ASP PRO ALA ARG THR LEU LEU ASP ILE
SEQRES 83 A 1151 ALA ARG LEU ARG GLN GLN ALA GLN LYS LEU GLY ILE ARG
SEQRES 84 A 1151 LYS LEU GLU GLY ASN GLU LYS GLY GLY VAL ILE GLU PHE
SEQRES 85 A 1151 ALA GLU LYS ASN HIS VAL ASN PRO ALA TRP LEU ILE GLY
SEQRES 86 A 1151 LEU LEU GLN LYS GLN PRO GLN HIS TYR ARG LEU ASP GLY
SEQRES 87 A 1151 PRO THR ARG LEU LYS PHE ILE GLN ASP LEU SER GLU ARG
SEQRES 88 A 1151 LYS THR ARG ILE GLU TRP VAL ARG GLN PHE MET ARG GLU
SEQRES 89 A 1151 LEU GLU GLU ASN ALA ILE ALA
SEQRES 1 B 1151 GLY PRO HIS MET PRO GLU GLN TYR ARG TYR THR LEU PRO
SEQRES 2 B 1151 VAL LYS ALA GLY GLU GLN ARG LEU LEU GLY GLU LEU THR
SEQRES 3 B 1151 GLY ALA ALA CYS ALA THR LEU VAL ALA GLU ILE ALA GLU
SEQRES 4 B 1151 ARG HIS ALA GLY PRO VAL VAL LEU ILE ALA PRO ASP MET
SEQRES 5 B 1151 GLN ASN ALA LEU ARG LEU HIS ASP GLU ILE SER GLN PHE
SEQRES 6 B 1151 THR ASP GLN MET VAL MET ASN LEU ALA ASP TRP GLU THR
SEQRES 7 B 1151 LEU PRO TYR ASP SER PHE SER PRO HIS GLN ASP ILE ILE
SEQRES 8 B 1151 SER SER ARG LEU SER THR LEU TYR GLN LEU PRO THR MET
SEQRES 9 B 1151 GLN ARG GLY VAL LEU ILE VAL PRO VAL ASN THR LEU MET
SEQRES 10 B 1151 GLN ARG VAL CYS PRO HIS SER PHE LEU HIS GLY HIS ALA
SEQRES 11 B 1151 LEU VAL MET LYS LYS GLY GLN ARG LEU SER ARG ASP ALA
SEQRES 12 B 1151 LEU ARG THR GLN LEU ASP SER ALA GLY TYR ARG HIS VAL
SEQRES 13 B 1151 ASP GLN VAL MET GLU HIS GLY GLU TYR ALA THR ARG GLY
SEQRES 14 B 1151 ALA LEU LEU ASP LEU PHE PRO MET GLY SER GLU LEU PRO
SEQRES 15 B 1151 TYR ARG LEU ASP PHE PHE ASP ASP GLU ILE ASP SER LEU
SEQRES 16 B 1151 ARG VAL PHE ASP VAL ASP SER GLN ARG THR LEU GLU GLU
SEQRES 17 B 1151 VAL GLU ALA ILE ASN LEU LEU PRO ALA HIS GLU PHE PRO
SEQRES 18 B 1151 THR ASP LYS ALA ALA ILE GLU LEU PHE ARG SER GLN TRP
SEQRES 19 B 1151 ARG ASP THR PHE GLU VAL LYS ARG ASP PRO GLU HIS ILE
SEQRES 20 B 1151 TYR GLN GLN VAL SER LYS GLY THR LEU PRO ALA GLY ILE
SEQRES 21 B 1151 GLU TYR TRP GLN PRO LEU PHE PHE SER GLU PRO LEU PRO
SEQRES 22 B 1151 PRO LEU PHE SER TYR PHE PRO ALA ASN THR LEU LEU VAL
SEQRES 23 B 1151 ASN THR GLY ASP LEU GLU THR SER ALA GLU ARG PHE GLN
SEQRES 24 B 1151 ALA ASP THR LEU ALA ARG PHE GLU ASN ARG GLY VAL ASP
SEQRES 25 B 1151 PRO MET ARG PRO LEU LEU PRO PRO GLN SER LEU TRP LEU
SEQRES 26 B 1151 ARG VAL ASP GLU LEU PHE SER GLU LEU LYS ASN TRP PRO
SEQRES 27 B 1151 ARG VAL GLN LEU LYS THR GLU HIS LEU PRO THR LYS ALA
SEQRES 28 B 1151 ALA ASN ALA ASN LEU GLY PHE GLN LYS LEU PRO ASP LEU
SEQRES 29 B 1151 ALA VAL GLN ALA GLN GLN LYS ALA PRO LEU ASP ALA LEU
SEQRES 30 B 1151 ARG LYS PHE LEU GLU THR PHE ASP GLY PRO VAL VAL PHE
SEQRES 31 B 1151 SER VAL GLU SER GLU GLY ARG ARG GLU ALA LEU GLY GLU
SEQRES 32 B 1151 LEU LEU ALA ARG ILE LYS ILE ALA PRO GLN ARG ILE MET
SEQRES 33 B 1151 ARG LEU ASP GLU ALA SER ASP ARG GLY ARG TYR LEU MET
SEQRES 34 B 1151 ILE GLY ALA ALA GLU HIS GLY PHE VAL ASP THR VAL ARG
SEQRES 35 B 1151 ASN LEU ALA LEU ILE CYS GLU SER ASP LEU LEU GLY GLU
SEQRES 36 B 1151 ARG VAL ALA ARG ARG ARG GLN ASP SER ARG ARG THR ILE
SEQRES 37 B 1151 ASN PRO ASP THR LEU ILE ARG ASN LEU ALA GLU LEU HIS
SEQRES 38 B 1151 ILE GLY GLN PRO VAL VAL HIS LEU GLU HIS GLY VAL GLY
SEQRES 39 B 1151 ARG TYR ALA GLY MET THR THR LEU GLU ALA GLY GLY ILE
SEQRES 40 B 1151 THR GLY GLU TYR LEU MET LEU THR TYR ALA ASN ASP ALA
SEQRES 41 B 1151 LYS LEU TYR VAL PRO VAL SER SER LEU HIS LEU ILE SER
SEQRES 42 B 1151 ARG TYR ALA GLY GLY ALA GLU GLU ASN ALA PRO LEU HIS
SEQRES 43 B 1151 LYS LEU GLY GLY ASP ALA TRP SER ARG ALA ARG GLN LYS
SEQRES 44 B 1151 ALA ALA GLU LYS VAL ARG ASP VAL ALA ALA GLU LEU LEU
SEQRES 45 B 1151 ASP ILE TYR ALA GLN ARG ALA ALA LYS GLU GLY PHE ALA
SEQRES 46 B 1151 PHE LYS HIS ASP ARG GLU GLN TYR GLN LEU PHE CYS ASP
SEQRES 47 B 1151 SER PHE PRO PHE GLU THR THR PRO ASP GLN ALA GLN ALA
SEQRES 48 B 1151 ILE ASN ALA VAL LEU SER ASP MET CYS GLN PRO LEU ALA
SEQRES 49 B 1151 MET ASP ARG LEU VAL CYS GLY ASP VAL GLY PHE GLY LYS
SEQRES 50 B 1151 THR GLU VAL ALA MET ARG ALA ALA PHE LEU ALA VAL ASP
SEQRES 51 B 1151 ASN HIS LYS GLN VAL ALA VAL LEU VAL PRO THR THR LEU
SEQRES 52 B 1151 LEU ALA GLN GLN HIS TYR ASP ASN PHE ARG ASP ARG PHE
SEQRES 53 B 1151 ALA ASN TRP PRO VAL ARG ILE GLU MET ILE SER ARG PHE
SEQRES 54 B 1151 ARG SER ALA LYS GLU GLN THR GLN ILE LEU ALA GLU VAL
SEQRES 55 B 1151 ALA GLU GLY LYS ILE ASP ILE LEU ILE GLY THR HIS LYS
SEQRES 56 B 1151 LEU LEU GLN SER ASP VAL LYS PHE LYS ASP LEU GLY LEU
SEQRES 57 B 1151 LEU ILE VAL ASP GLU GLU HIS ARG PHE GLY VAL ARG HIS
SEQRES 58 B 1151 LYS GLU ARG ILE LYS ALA MET ARG ALA ASN VAL ASP ILE
SEQRES 59 B 1151 LEU THR LEU THR ALA THR PRO ILE PRO ARG THR LEU ASN
SEQRES 60 B 1151 MET ALA MET SER GLY MET ARG ASP LEU SER ILE ILE ALA
SEQRES 61 B 1151 THR PRO PRO ALA ARG ARG LEU ALA VAL LYS THR PHE VAL
SEQRES 62 B 1151 ARG GLU TYR ASP SER MET VAL VAL ARG GLU ALA ILE LEU
SEQRES 63 B 1151 ARG GLU ILE LEU ARG GLY GLY GLN VAL TYR TYR LEU TYR
SEQRES 64 B 1151 ASN ASP VAL GLU ASN ILE GLN LYS ALA ALA GLU ARG LEU
SEQRES 65 B 1151 ALA GLU LEU VAL PRO GLU ALA ARG ILE ALA ILE GLY HIS
SEQRES 66 B 1151 GLY GLN MET ARG GLU ARG GLU LEU GLU ARG VAL MET ASN
SEQRES 67 B 1151 ASP PHE HIS HIS GLN ARG PHE ASN VAL LEU VAL CYS THR
SEQRES 68 B 1151 THR ILE ILE GLU THR GLY ILE ASP ILE PRO THR ALA ASN
SEQRES 69 B 1151 THR ILE ILE ILE GLU ARG ALA ASP HIS PHE GLY LEU ALA
SEQRES 70 B 1151 GLN LEU HIS GLN LEU ARG GLY ARG VAL GLY ARG SER HIS
SEQRES 71 B 1151 HIS GLN ALA TYR ALA TRP LEU LEU THR PRO HIS PRO LYS
SEQRES 72 B 1151 ALA MET THR THR ASP ALA GLN LYS ARG LEU GLU ALA ILE
SEQRES 73 B 1151 ALA SER LEU GLU ASP LEU GLY ALA GLY PHE ALA LEU ALA
SEQRES 74 B 1151 THR HIS ASP LEU GLU ILE ARG GLY ALA GLY GLU LEU LEU
SEQRES 75 B 1151 GLY GLU GLU GLN SER GLY SER MET GLU THR ILE GLY PHE
SEQRES 76 B 1151 SER LEU TYR MET GLU LEU LEU GLU ASN ALA VAL ASP ALA
SEQRES 77 B 1151 LEU LYS ALA GLY ARG GLU PRO SER LEU GLU ASP LEU THR
SEQRES 78 B 1151 SER GLN GLN THR GLU VAL GLU LEU ARG MET PRO SER LEU
SEQRES 79 B 1151 LEU PRO ASP ASP PHE ILE PRO ASP VAL ASN THR ARG LEU
SEQRES 80 B 1151 SER PHE TYR LYS ARG ILE ALA SER ALA LYS THR GLU ASN
SEQRES 81 B 1151 GLU LEU GLU GLU ILE LYS VAL GLU LEU ILE ASP ARG PHE
SEQRES 82 B 1151 GLY LEU LEU PRO ASP PRO ALA ARG THR LEU LEU ASP ILE
SEQRES 83 B 1151 ALA ARG LEU ARG GLN GLN ALA GLN LYS LEU GLY ILE ARG
SEQRES 84 B 1151 LYS LEU GLU GLY ASN GLU LYS GLY GLY VAL ILE GLU PHE
SEQRES 85 B 1151 ALA GLU LYS ASN HIS VAL ASN PRO ALA TRP LEU ILE GLY
SEQRES 86 B 1151 LEU LEU GLN LYS GLN PRO GLN HIS TYR ARG LEU ASP GLY
SEQRES 87 B 1151 PRO THR ARG LEU LYS PHE ILE GLN ASP LEU SER GLU ARG
SEQRES 88 B 1151 LYS THR ARG ILE GLU TRP VAL ARG GLN PHE MET ARG GLU
SEQRES 89 B 1151 LEU GLU GLU ASN ALA ILE ALA
HET SO4 A1149 5
HET SO4 A1150 5
HET EPE A1151 15
HET EPE A1152 15
HET SO4 B1149 5
HET EPE B1150 15
HET EPE B1151 15
HET EPE B1152 15
HETNAM SO4 SULFATE ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 5 EPE 5(C8 H18 N2 O4 S)
FORMUL 11 HOH *120(H2 O)
HELIX 1 1 ALA A 25 ARG A 37 1 13
HELIX 2 2 ASP A 48 SER A 60 1 13
HELIX 3 3 GLN A 61 THR A 63 5 3
HELIX 4 4 HIS A 84 LEU A 98 1 15
HELIX 5 5 PRO A 99 MET A 101 5 3
HELIX 6 6 VAL A 110 MET A 114 1 5
HELIX 7 7 PRO A 119 HIS A 126 1 8
HELIX 8 8 SER A 137 GLY A 149 1 13
HELIX 9 9 ASP A 220 PHE A 235 1 16
HELIX 10 10 HIS A 243 LYS A 250 1 8
HELIX 11 11 GLY A 256 PHE A 265 5 10
HELIX 12 12 PRO A 271 PHE A 276 5 6
HELIX 13 13 ASP A 287 ARG A 306 1 20
HELIX 14 14 PRO A 316 TRP A 321 1 6
HELIX 15 15 ARG A 323 LYS A 332 1 10
HELIX 16 16 LEU A 371 GLU A 379 1 9
HELIX 17 17 SER A 391 ALA A 403 1 13
HELIX 18 18 ARG A 404 LYS A 406 5 3
HELIX 19 19 ARG A 414 ALA A 418 5 5
HELIX 20 20 GLU A 446 LEU A 450 1 5
HELIX 21 21 ASP A 460 THR A 464 5 5
HELIX 22 22 ASN A 466 ASN A 473 1 8
HELIX 23 23 ALA A 514 ASP A 516 5 3
HELIX 24 24 SER A 524 HIS A 527 5 4
HELIX 25 25 ASP A 548 ALA A 577 1 30
HELIX 26 26 ASP A 586 SER A 596 1 11
HELIX 27 27 THR A 602 GLN A 618 1 17
HELIX 28 28 THR A 635 ASP A 647 1 13
HELIX 29 29 THR A 658 PHE A 673 1 16
HELIX 30 30 SER A 688 GLU A 701 1 14
HELIX 31 31 HIS A 711 SER A 716 1 6
HELIX 32 32 GLU A 731 PHE A 734 5 4
HELIX 33 33 GLY A 735 ALA A 747 1 13
HELIX 34 34 PRO A 760 SER A 768 1 9
HELIX 35 35 ASP A 794 LEU A 807 1 14
HELIX 36 36 ASN A 821 VAL A 833 1 13
HELIX 37 37 ARG A 846 HIS A 859 1 14
HELIX 38 38 ILE A 871 ILE A 875 5 5
HELIX 39 39 GLY A 892 GLY A 901 1 10
HELIX 40 40 HIS A 918 MET A 922 5 5
HELIX 41 41 THR A 923 ALA A 934 1 12
HELIX 42 42 GLY A 940 GLY A 960 1 21
HELIX 43 43 GLY A 960 GLY A 971 1 12
HELIX 44 44 GLY A 971 GLY A 989 1 19
HELIX 45 45 LEU A 994 THR A 998 5 5
HELIX 46 46 ASP A 1019 ALA A 1033 1 15
HELIX 47 47 THR A 1035 GLY A 1051 1 17
HELIX 48 48 PRO A 1054 GLY A 1074 1 21
HELIX 49 49 ASN A 1096 GLN A 1107 1 12
HELIX 50 50 GLU A 1127 GLU A 1144 1 18
HELIX 51 51 ALA B 25 ARG B 37 1 13
HELIX 52 52 ASP B 48 THR B 63 1 16
HELIX 53 53 HIS B 84 LEU B 98 1 15
HELIX 54 54 VAL B 110 MET B 114 1 5
HELIX 55 55 PRO B 119 HIS B 124 1 6
HELIX 56 56 SER B 137 ALA B 148 1 12
HELIX 57 57 ASP B 220 ASP B 233 1 14
HELIX 58 58 HIS B 243 LYS B 250 1 8
HELIX 59 59 GLY B 256 PHE B 265 5 10
HELIX 60 60 PRO B 271 PHE B 276 5 6
HELIX 61 61 ASP B 287 GLY B 307 1 21
HELIX 62 62 ARG B 323 GLU B 330 1 8
HELIX 63 63 LEU B 371 PHE B 381 1 11
HELIX 64 64 SER B 391 ALA B 403 1 13
HELIX 65 65 ASN B 466 ARG B 472 1 7
HELIX 66 66 ALA B 514 ASP B 516 5 3
HELIX 67 67 SER B 524 ILE B 529 5 6
HELIX 68 68 ASP B 548 LYS B 578 1 31
HELIX 69 69 ASP B 586 CYS B 594 1 9
HELIX 70 70 ASP B 595 PHE B 597 5 3
HELIX 71 71 THR B 602 GLN B 618 1 17
HELIX 72 72 THR B 635 ASN B 648 1 14
HELIX 73 73 THR B 658 PHE B 673 1 16
HELIX 74 74 SER B 688 GLU B 701 1 14
HELIX 75 75 HIS B 711 LEU B 714 5 4
HELIX 76 76 GLU B 731 PHE B 734 5 4
HELIX 77 77 VAL B 736 ALA B 747 1 12
HELIX 78 78 PRO B 760 SER B 768 1 9
HELIX 79 79 MET B 796 LEU B 807 1 12
HELIX 80 80 ASN B 821 GLU B 831 1 11
HELIX 81 81 ARG B 846 HIS B 859 1 14
HELIX 82 82 ILE B 871 ILE B 875 5 5
HELIX 83 83 GLY B 892 VAL B 903 1 12
HELIX 84 84 HIS B 918 MET B 922 5 5
HELIX 85 85 ASP B 925 SER B 935 1 11
HELIX 86 86 GLY B 940 GLY B 960 1 21
HELIX 87 87 GLY B 960 GLY B 971 1 12
HELIX 88 88 GLY B 971 LYS B 987 1 17
HELIX 89 89 LEU B 994 THR B 998 5 5
HELIX 90 90 ASP B 1019 ALA B 1033 1 15
HELIX 91 91 THR B 1035 GLY B 1051 1 17
HELIX 92 92 PRO B 1054 GLY B 1074 1 21
HELIX 93 93 ASN B 1096 GLN B 1107 1 12
HELIX 94 94 GLU B 1127 ASN B 1145 1 19
SHEET 1 A 5 VAL A 67 ASN A 69 0
SHEET 2 A 5 GLY A 104 PRO A 109 1 O VAL A 105 N MET A 68
SHEET 3 A 5 PRO A 41 ALA A 46 1 N LEU A 44 O LEU A 106
SHEET 4 A 5 LEU A 281 THR A 285 1 O VAL A 283 N VAL A 43
SHEET 5 A 5 ARG A 336 LEU A 339 1 O VAL A 337 N ASN A 284
SHEET 1 B 2 LEU A 128 LYS A 131 0
SHEET 2 B 2 ALA A 208 LEU A 211 -1 O LEU A 211 N LEU A 128
SHEET 1 C 6 ARG A 151 VAL A 153 0
SHEET 2 C 6 GLU A 161 ARG A 165 1 O TYR A 162 N VAL A 153
SHEET 3 C 6 LEU A 168 LEU A 171 -1 O ASP A 170 N ALA A 163
SHEET 4 C 6 TYR A 180 ARG A 181 -1 O TYR A 180 N LEU A 171
SHEET 5 C 6 LEU A 192 PHE A 195 -1 O ARG A 193 N ARG A 181
SHEET 6 C 6 THR A 202 VAL A 206 -1 O VAL A 206 N LEU A 192
SHEET 1 D 2 PHE A 184 PHE A 185 0
SHEET 2 D 2 GLU A 188 ILE A 189 -1 O GLU A 188 N PHE A 185
SHEET 1 E 6 PHE A 355 GLN A 356 0
SHEET 2 E 6 PHE A 434 ASP A 436 -1 O VAL A 435 N GLN A 356
SHEET 3 E 6 LEU A 441 CYS A 445 -1 O LEU A 441 N ASP A 436
SHEET 4 E 6 PHE A 387 VAL A 389 1 N SER A 388 O ILE A 444
SHEET 5 E 6 TYR A 424 ILE A 427 1 O TYR A 424 N PHE A 387
SHEET 6 E 6 GLN A 410 ARG A 411 1 N GLN A 410 O LEU A 425
SHEET 1 F 5 LYS A 518 PRO A 522 0
SHEET 2 F 5 THR A 505 THR A 512 -1 N LEU A 511 O LEU A 519
SHEET 3 F 5 GLY A 489 GLU A 500 -1 N GLY A 495 O MET A 510
SHEET 4 F 5 PRO A 482 HIS A 485 -1 N HIS A 485 O GLY A 489
SHEET 5 F 5 ILE A 529 ARG A 531 -1 O SER A 530 N VAL A 484
SHEET 1 G 7 ILE A 680 ILE A 683 0
SHEET 2 G 7 ILE A 706 GLY A 709 1 O ILE A 708 N ILE A 683
SHEET 3 G 7 GLN A 651 LEU A 655 1 N VAL A 652 O LEU A 707
SHEET 4 G 7 LEU A 723 ASP A 729 1 O LEU A 725 N ALA A 653
SHEET 5 G 7 ASP A 750 THR A 755 1 O LEU A 754 N VAL A 728
SHEET 6 G 7 ASP A 623 CYS A 627 1 N ARG A 624 O THR A 753
SHEET 7 G 7 ASP A 772 ILE A 775 1 O SER A 774 N LEU A 625
SHEET 1 H 6 VAL A 786 GLU A 792 0
SHEET 2 H 6 ALA A 910 THR A 916 1 O LEU A 914 N PHE A 789
SHEET 3 H 6 ALA A 880 ILE A 885 1 N ASN A 881 O TYR A 911
SHEET 4 H 6 GLN A 811 LEU A 815 1 N TYR A 813 O THR A 882
SHEET 5 H 6 VAL A 864 CYS A 867 1 O LEU A 865 N VAL A 812
SHEET 6 H 6 ILE A 838 ILE A 840 1 N ALA A 839 O VAL A 866
SHEET 1 I 5 VAL A1004 GLU A1005 0
SHEET 2 I 5 LEU A1078 GLY A1080 1 O GLY A1080 N GLU A1005
SHEET 3 I 5 GLY A1084 GLU A1088 -1 O VAL A1086 N GLU A1079
SHEET 4 I 5 ARG A1118 ILE A1122 -1 O PHE A1121 N GLY A1085
SHEET 5 I 5 TYR A1111 ASP A1114 -1 N ARG A1112 O LYS A1120
SHEET 1 J 4 VAL B 67 ASN B 69 0
SHEET 2 J 4 GLY B 104 PRO B 109 1 O VAL B 105 N MET B 68
SHEET 3 J 4 PRO B 41 ALA B 46 1 N VAL B 42 O GLY B 104
SHEET 4 J 4 LEU B 281 ASN B 284 1 O VAL B 283 N ILE B 45
SHEET 1 K 2 LEU B 128 LYS B 131 0
SHEET 2 K 2 ALA B 208 LEU B 211 -1 O LEU B 211 N LEU B 128
SHEET 1 L 6 ARG B 151 VAL B 153 0
SHEET 2 L 6 GLU B 161 ARG B 165 1 O TYR B 162 N VAL B 153
SHEET 3 L 6 LEU B 168 LEU B 171 -1 O ASP B 170 N ALA B 163
SHEET 4 L 6 TYR B 180 PHE B 184 -1 O TYR B 180 N LEU B 171
SHEET 5 L 6 ILE B 189 PHE B 195 -1 O ARG B 193 N ARG B 181
SHEET 6 L 6 THR B 202 VAL B 206 -1 O VAL B 206 N LEU B 192
SHEET 1 M 5 PHE B 355 GLN B 356 0
SHEET 2 M 5 PHE B 434 ASP B 436 -1 O VAL B 435 N GLN B 356
SHEET 3 M 5 LEU B 441 LEU B 443 -1 O LEU B 443 N PHE B 434
SHEET 4 M 5 VAL B 385 VAL B 389 1 N VAL B 386 O ALA B 442
SHEET 5 M 5 LEU B 425 ILE B 427 1 O MET B 426 N VAL B 389
SHEET 1 N 4 PRO B 482 HIS B 485 0
SHEET 2 N 4 GLY B 489 GLU B 500 -1 O GLY B 489 N HIS B 485
SHEET 3 N 4 THR B 505 THR B 512 -1 O THR B 512 N ARG B 492
SHEET 4 N 4 LYS B 518 PRO B 522 -1 O VAL B 521 N LEU B 509
SHEET 1 O 7 ILE B 680 ILE B 683 0
SHEET 2 O 7 ILE B 706 GLY B 709 1 O ILE B 708 N GLU B 681
SHEET 3 O 7 GLN B 651 LEU B 655 1 N VAL B 654 O GLY B 709
SHEET 4 O 7 LEU B 723 ASP B 729 1 O ILE B 727 N ALA B 653
SHEET 5 O 7 ASP B 750 THR B 755 1 O LEU B 752 N VAL B 728
SHEET 6 O 7 ASP B 623 CYS B 627 1 N ARG B 624 O THR B 753
SHEET 7 O 7 ASP B 772 ILE B 775 1 O SER B 774 N LEU B 625
SHEET 1 P 6 VAL B 786 GLU B 792 0
SHEET 2 P 6 ALA B 910 THR B 916 1 O LEU B 914 N PHE B 789
SHEET 3 P 6 THR B 882 ILE B 885 1 N ILE B 883 O TRP B 913
SHEET 4 P 6 VAL B 812 LEU B 815 1 N LEU B 815 O ILE B 884
SHEET 5 P 6 VAL B 864 CYS B 867 1 O LEU B 865 N VAL B 812
SHEET 6 P 6 ILE B 838 GLY B 841 1 N ALA B 839 O VAL B 866
SHEET 1 Q 4 ILE B1075 ASN B1081 0
SHEET 2 Q 4 GLY B1084 PHE B1089 -1 O GLU B1088 N LYS B1077
SHEET 3 Q 4 ARG B1118 ILE B1122 -1 O LEU B1119 N ILE B1087
SHEET 4 Q 4 TYR B1111 ASP B1114 -1 N ARG B1112 O LYS B1120
SITE 1 AC1 5 THR A 658 THR A 659 LEU A 660 ARG A 685
SITE 2 AC1 5 HIS B 842
SITE 1 AC2 2 ARG A 395 ARG A 411
SITE 1 AC3 2 ARG B 395 ARG B 411
SITE 1 AC4 8 HIS A 842 THR B 658 THR B 659 LEU B 660
SITE 2 AC4 8 ARG B 685 THR B 710 HIS B 711 LYS B 712
SITE 1 AC5 11 HIS A 897 ARG A 900 LEU A 936 GLU A 937
SITE 2 AC5 11 ASP A 938 LEU A 939 GLY A 940 ALA A 941
SITE 3 AC5 11 GLY A 942 PHE A 943 HOH A1166
SITE 1 AC6 10 HIS B 897 ARG B 900 LEU B 936 GLU B 937
SITE 2 AC6 10 ASP B 938 LEU B 939 GLY B 940 ALA B 941
SITE 3 AC6 10 GLY B 942 PHE B 943
SITE 1 AC7 6 GLN A 459 ARG A 462 ARG A 782 ARG A 905
SITE 2 AC7 6 SER A 906 HIS A 907
SITE 1 AC8 5 SER B 461 ARG B 782 ARG B 905 SER B 906
SITE 2 AC8 5 HIS B 907
CRYST1 151.870 161.990 161.730 90.00 105.09 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006585 0.000000 0.001775 0.00000
SCALE2 0.000000 0.006173 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END